ID   PAT_ALCFA               Reviewed;         197 AA.
AC   P31668;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Phosphinothricin N-acetyltransferase {ECO:0000250|UniProtKB:Q57146};
DE            Short=PPT N-acetyltransferase {ECO:0000250|UniProtKB:Q57146};
DE            EC=2.3.1.183 {ECO:0000250|UniProtKB:Q57146};
DE   AltName: Full=Phosphinothricin-resistance protein {ECO:0000303|Ref.1};
GN   Name=pat;
OS   Alcaligenes faecalis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=511;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Brauer D., Bartsch K., Donn G.;
RT   "Gene resistant to phosphinothricin.";
RL   Patent number EP0290986, 17-NOV-1988.
CC   -!- FUNCTION: Inactivates phosphinothricin (PPT) by transfer of an acetyl
CC       group from acetyl CoA. This enzyme is an effector of phosphinothricin
CC       tripeptide (PTT or bialaphos) resistance.
CC       {ECO:0000250|UniProtKB:Q57146}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + phosphinothricin = CoA + H(+) + N-
CC         acetylphosphinothricin; Xref=Rhea:RHEA:12597, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58879,
CC         ChEBI:CHEBI:58882; EC=2.3.1.183;
CC         Evidence={ECO:0000250|UniProtKB:Q57146};
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. PAT/BAR subfamily.
CC       {ECO:0000305}.
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DR   EMBL; A01504; CAA00175.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P31668; -.
DR   SMR; P31668; -.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0102971; F:phosphinothricin N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Antibiotic resistance; Herbicide resistance; Transferase.
FT   CHAIN           1..197
FT                   /note="Phosphinothricin N-acetyltransferase"
FT                   /id="PRO_0000074572"
FT   DOMAIN          26..189
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   BINDING         110..112
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
FT   BINDING         118..123
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
FT   BINDING         150
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ZPD3"
SQ   SEQUENCE   197 AA;  21213 MW;  ACA6E3B51AA55FE3 CRC64;
     MPSSSSHPST PDAPQRVGVE LARCACTVRV VRDDDLPAIT AIYAHHVRTG TASFEEVPPD
     DTEMRARCAK VLDAGLPYLV AERDGKLLGY AYATHYRPRS AYRFTLEDSV YIAPDAIGQG
     VGRTLLLTLI ARCEGGPWRQ LIANVGDSGN TASLGLHAAC GFVQAGVLKS VGFKFGRWID
     TVLMQRPLNA GDTTLPE